Journal article
Amphipathic α-helical peptide, HP (2-20), and its analogues derived from Helicobacter pylori: Pore formation mechanism in various lipid compositions
SC Park, MH Kim, MA Hossain, SY Shin, Y Kim, L Stella, JD Wade, Y Park, KS Hahm
Biochimica Et Biophysica Acta Biomembranes | ELSEVIER SCIENCE BV | Published : 2008
Abstract
In a previous study, we determined that HP(2-20) (residues 2-20 of parental HP derived from the N-terminus of Helicobacter pylori Ribosomal Protein L1) and its analogue, HPA3, exhibit broad-spectrum antimicrobial activity. The primary objective of the present study was to gain insight into the relevant mechanisms of action using analogues of HP(2-20) together with model liposomes of various lipid compositions and electron microscopy. We determined that these analogues, HPA3 and HPA3NT3, exert potent antibacterial effects in low-salt buffer and antifungal activity against chitin-containing fungi, while having little or no hemolytic activity or cytotoxicity against mammalian cell lines. Our ex..
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